Abstract
Using the chick embryo pelvis cartilage sulfatation factor activity as assay, the authors have followed the purification of the “small form” of human somatomedin A. The starting material has been the Cohn IV fraction. The following technics have been used : - Acidic ethanol extraction and acetone extraction (a 30 fold purification obtained). - Phenol extraction (no results for phenol inhibits the bioassay). - CM 52 cellulose chromatography in batchwise system (a 300 fold purification obtained). - Isolation of peptides of M.W. between 10 000 and 1 000 by preparative ultrafiltration on Millipore apparatus (a 800 to 1 200 fold purification obtained). - HPLC chromatographic in volatil buffer and acetonitril gradient : the activity is recovered in only one fraction which appears at 60 p. cent acetonitril.
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Straczek, J., Heulin, M., Belleville, F. et al. PURIFICATION Of THE “SMALL FORM” OF HUMAN SOMATOMEDIN A. Pediatr Res 15, 87 (1981). https://doi.org/10.1203/00006450-198101000-00099
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DOI: https://doi.org/10.1203/00006450-198101000-00099